PMID- 22791285
OWN - NLM
STAT- MEDLINE
DCOM- 20121127
LR  - 20211203
IS  - 1528-0020 (Electronic)
IS  - 0006-4971 (Linking)
VI  - 120
IP  - 10
DP  - 2012 Sep 6
TI  - Internalization and endosomal degradation of receptor-bound antigens regulate the 
      efficiency of cross presentation by human dendritic cells.
PG  - 2011-20
LID - 10.1182/blood-2012-01-402370 [doi]
AB  - Dendritic cells (DCs) can capture extracellular antigens and load resultant 
      peptides on to MHC class I molecules, a process termed cross presentation. The 
      mechanisms of cross presentation remain incompletely understood, particularly in 
      primary human DCs. One unknown is the extent to which antigen delivery to 
      distinct endocytic compartments determines cross presentation efficiency, 
      possibly by influencing antigen egress to the cytosol. We addressed the problem 
      directly and quantitatively by comparing the cross presentation of identical 
      antigens conjugated with antibodies against different DC receptors that are 
      targeted to early or late endosomes at distinct efficiencies. In human BDCA1+ and 
      monocyte-derived DCs, CD40 and mannose receptor targeted antibody conjugates to 
      early endosomes, whereas DEC205 targeted antigen primarily to late compartments. 
      Surprisingly, the receptor least efficient at internalization, CD40, was the most 
      efficient at cross presentation. This did not reflect DC activation by CD40, but 
      rather its relatively poor uptake or intra-endosomal degradation compared with 
      mannose receptor or DEC205. Thus, although both early and late endosomes appear 
      to support cross presentation in human DCs, internalization efficiency, 
      especially to late compartments, may be a negative predictor of activity when 
      selecting receptors for vaccine development.
FAU - Chatterjee, Bithi
AU  - Chatterjee B
AD  - Department of Cell Biology, Yale University School of Medicine, New Haven, CT, 
      USA.
FAU - Smed-Sorensen, Anna
AU  - Smed-Sorensen A
FAU - Cohn, Lillian
AU  - Cohn L
FAU - Chalouni, Cecile
AU  - Chalouni C
FAU - Vandlen, Richard
AU  - Vandlen R
FAU - Lee, Byoung-Chul
AU  - Lee BC
FAU - Widger, Jenifer
AU  - Widger J
FAU - Keler, Tibor
AU  - Keler T
FAU - Delamarre, Lelia
AU  - Delamarre L
FAU - Mellman, Ira
AU  - Mellman I
LA  - eng
PT  - Journal Article
DEP - 20120712
PL  - United States
TA  - Blood
JT  - Blood
JID - 7603509
RN  - 0 (Antigen-Antibody Complex)
RN  - 0 (Antigens, CD)
RN  - 0 (CLEC4C protein, human)
RN  - 0 (DEC-205 receptor)
RN  - 0 (Histocompatibility Antigens Class I)
RN  - 0 (Lectins, C-Type)
RN  - 0 (Mannose Receptor)
RN  - 0 (Mannose-Binding Lectins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Minor Histocompatibility Antigens)
RN  - 0 (Peptides)
RN  - 0 (Receptors, Cell Surface)
RN  - 0 (Receptors, Immunologic)
SB  - IM
MH  - Amino Acid Sequence
MH  - Antigen-Antibody Complex/*immunology/metabolism
MH  - Antigens, CD/immunology/metabolism
MH  - *Cross-Priming
MH  - Dendritic Cells/cytology/*immunology/metabolism
MH  - Endocytosis/*immunology
MH  - Endosomes/*immunology/metabolism
MH  - Histocompatibility Antigens Class I/immunology/metabolism
MH  - Humans
MH  - Immunity, Innate
MH  - Lectins, C-Type/immunology/metabolism
MH  - Mannose Receptor
MH  - Mannose-Binding Lectins/immunology/metabolism
MH  - Membrane Glycoproteins/immunology/metabolism
MH  - Minor Histocompatibility Antigens
MH  - Molecular Sequence Data
MH  - Peptides/immunology/metabolism
MH  - Primary Cell Culture
MH  - Receptors, Cell Surface/immunology/metabolism
MH  - Receptors, Immunologic/immunology/metabolism
EDAT- 2012/07/14 06:00
MHDA- 2012/12/10 06:00
CRDT- 2012/07/14 06:00
PHST- 2012/07/14 06:00 [entrez]
PHST- 2012/07/14 06:00 [pubmed]
PHST- 2012/12/10 06:00 [medline]
AID - S0006-4971(20)46429-8 [pii]
AID - 10.1182/blood-2012-01-402370 [doi]
PST - ppublish
SO  - Blood. 2012 Sep 6;120(10):2011-20. doi: 10.1182/blood-2012-01-402370. Epub 2012 
      Jul 12.